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Q30350967-004E13CC-EF64-4E6B-886A-B66E883FBD66
Q30350967-004E13CC-EF64-4E6B-886A-B66E883FBD66
BestRank
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http://www.wikidata.org/entity/statement/Q30350967-004E13CC-EF64-4E6B-886A-B66E883FBD66
Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics
P2860
Q30350967-004E13CC-EF64-4E6B-886A-B66E883FBD66
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30350967-004E13CC-EF64-4E6B-886A-B66E883FBD66
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wasDerivedFrom
b6330e6ae6ddded56408f9659e8a64ee2d5ccd10
P2860
Heat-induced aggregation of recombinant erythropoietin in the intact and deglycosylated states as monitored by gel permeation chromatography combined with a low-angle laser light scattering technique.